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The sedolisin family of peptidases are a family of serine proteases structurally related to the subtilisin (S8) family. Well-known members of this family include sedolisin ("pseudomonalisin") found in Pseudomonas bacteria, xanthomonalisin ("sedolisin-B"), physarolisin as well as animal tripeptidyl peptidase I. It is also known as sedolysin or serine-carboxyl peptidase. This group of enzymes contains a variation on the catalytic triad: unlike S8 which uses Ser-His-Asp, this group runs on Ser-Glu-Asp, with an additional acidic residue Asp in the oxyanion hole.
References
- ↑ Kobayashi H, Kusakabe I, Murakami K (1983). "Substrate specificity of a carboxyl proteinase from Irpex lacteus". Agric. Biol. Chem. 47 (8): 1921–1923. doi: 10.1271/bbb1961.47.1921 .
- ↑ Kobayashi H, Sekibata S, Shibuya H, Yoshida S, Kusakabe I, Murakami K (1989). "Cloning and sequence analysis of cDNA for Irpex lacteus aspartic proteinase". Agric. Biol. Chem. 53 (7): 1927–1933. doi: 10.1271/bbb1961.53.1927 .
